| http://purl.uniprot.org/citations/9606181 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9606181 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9606181 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/9606181 | http://www.w3.org/2000/01/rdf-schema#comment | "Vps4p is an AAA-type ATPase required for efficient transport of biosynthetic and endocytic cargo from an endosome to the lysosome-like vacuole of Saccharomyces cerevisiae. Vps4p mutants that do not bind ATP or are defective in ATP hydrolysis were characterized both in vivo and in vitro. The nucleotide-free or ADP-bound form of Vps4p existed as a dimer, whereas in the ATP-locked state, Vps4p dimers assembled into a decameric complex. This suggests that ATP hydrolysis drives a cycle of association and dissociation of Vps4p dimers/decamers. Nucleotide binding also regulated the association of Vps4p with an endosomal compartment in vivo. This membrane association required the N-terminal coiled-coil motif of Vps4p, but deletion of the coiled-coil domain did not affect ATPase activity or oligomeric assembly of the protein. Membrane association of two previously uncharacterized class E Vps proteins, Vps24p and Vps32p/Snf7p, was also affected by mutations in VPS4. Upon inactivation of a temperature-conditional vps4 mutant, Vps24p and Vps32p/Snf7p rapidly accumulated in a large membrane-bound complex. Immunofluorescence indicated that both proteins function with Vps4p at a common endosomal compartment. Together, the data suggest that the Vps4 ATPase catalyzes the release (uncoating) of an endosomal membrane-associated class E protein complex(es) required for normal morphology and sorting activity of the endosome."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.11.2982"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.org/dc/terms/identifier | "doi:10.1093/emboj/17.11.2982"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Emr S.D."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Emr S.D."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Babst M."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Babst M."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Wendland B."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Wendland B."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Estepa E.J."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/author | "Estepa E.J."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/pages | "2982-2993"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/pages | "2982-2993"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/title | "The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/title | "The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function."xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/volume | "17"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://purl.uniprot.org/core/volume | "17"xsd:string |
| http://purl.uniprot.org/citations/9606181 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9606181 |